Z-Pro-OH

Z-Pro-OH

[Synthesis of N-alpha-(arylsulfonyl-L-prolyl)- and N alpha-(benzyloxycarbonyl-L-prolyl)-D,L-4-amidinophenylalanine amides as inhibitors of thrombin].[Pubmed:3725864]

Pharmazie. 1986 Apr;41(4):233-5.

N alpha substituted 4-cyanophenylalanines were prepared by reaction of the acid chloride, the activated ester and the mixed anhydride of Tos-Pro-OH, 2-naphthylsulfonyl-L-proline and Z-Pro-OH, respectively, with cyanophenylalanine. These acids were transferred into the amides via the 4-nitrophenyl esters or the mixed anhydrides. The cyano compounds were converted via the thioamides and the thioimidic esters into the amidines by common way. The exchange of the glycine residue by prolin in compounds former described caused a decreased antithrombin effect.

Thermolysin and alpha-chymotrypsin mediated synthesis of tripeptides containing proline.[Pubmed:3366545]

Int J Pept Protein Res. 1988 Feb;31(2):116-25.

The tripeptides Z-Pro-Leu-Gly-OEt, Z-Pro-Leu-Gly-NH2 and Z-Pro-Leu-Gly-OBzl were synthesized by thermolysin and alpha-chymotrypsin catalysis. The optimum conditions for the couplings between Z-Pro-OH and H-Leu-OEt or H-Leu-Gly-OEt catalysed by thermolysin were determined by a systematic study involving analysis of pH effect, ammonium sulfate concentration, reaction time, enzyme concentration, and relative proportion of the carboxyl and amine components. The best yield obtained for Z-Pro-Leu-OEt was 77% and for Z-Pro-Leu-Gly-OEt, 100%. Z-Pro-Leu-OEt was coupled to H-Gly-OEt, H-Gly-NH2 and H-Gly-OBzl. The best conditions to obtain Z-Pro-Leu-Gly-OEt and Z-Pro-Leu-Gly-NH2 were determined by the study of some factors that affect the reaction yield, such as organic solvent presence, substrate ratio and aqueous and organic solvent ratio. The yield obtained under optimum synthesis conditions was 55% for Z-Pro-Leu-Gly-OEt and 61% for Z-Pro-Leu-Gly-NH2. Z-Pro-Leu-Gly-OBzl was synthesized with 42% yield.

Synthesis of modified tuftsins containing monosaccharides or monosaccharide derivatives.[Pubmed:3570665]

Int J Pept Protein Res. 1987 Feb;29(2):250-61.

Synthesis of some modified tuftsins is described in which a monosaccharide or a monosaccharide derivative was incorporated in the molecule. Acylation of H-Thr-Lys(Z)-Pro-Arg(NO2)-OBzl with D(+)-gluco-1,5-lactone followed by catalytic hydrogenation gave N alpha-gluconyl-tuftsin. Glycosylation of the carboxyl function of the C-terminal arginine has been achieved by reacting, through the mixed anhydride procedure, Boc-Thr-Lys(Z)-Pro-OH with 2-deoxy-2-(NG-nitroargininamido)-D-glucopyranose followed by catalytic hydrogenation and trifluoroacetic acid treatment. O-Glucosyl-tuftsin has been prepared by reacting o-nitrophenyl N-benzyloxycarbonyl-O-[(alpha + beta) 2,3,4,6-tetra-O-benzyl-D-glucopyranosyl]-threoninate with H-Lys(Z)-Pro-Arg(NO2)-OBzl in the presence of 1-hydroxybenzotriazole. Flash chromatography on silica gel allowed a partial separation of the diastereoisomers, one of which has been isolated in a reasonable yield. The single diastereoisomer and the alpha + beta anomeric mixture were separately deblocked by catalytic hydrogenation and purified by RP-HPLC.

Synthesis, radiolabeling and biological activity of peptide oostatic hormone and its analogues.[Pubmed:9309578]

J Pept Res. 1997 Sep;50(3):153-8.

A series of Pro peptides containing the sequence of the oostatic hormone 3d and its shorter analogues 3a-3c differing in a number of the C-terminal Pro residues was prepared for a study of its effect on oogenesis in Sarcophaga bullata Parker (Diptera). Peptides 3a-3d were synthesized in solution by the fragment condensation of Boc-Tyr-Asp(OtBu)-Pro-Ala-Pro-OH (2f) with Pro oligopeptides H-(Pro)2-5-OtBu. The amino-terminal protected pentapeptide acid 2f was prepared by a stepwise procedure from TFA.H-Ala-Pro-OMe using Boc-Pro-OH, Z-Asp(OtBu)-OSu and Boc-Tyr-OSu. The H(Z)-(Pro)2-5-OtBu oligopeptides 1a-1h were synthesized from Z-Pro-OH and H-Pro-OtBu by a combination of stepwise procedure and fragment condensation. The 125I-labeled molecules of the octapeptide 3b and decapeptide 3d were used for radiotracer distribution studies. Evidence of content of the labeled peptide material in various parts of the insect body (ovaries, head, intestine) is presented. The time distribution of the labeled material in the insect organs was correlated with results of histological analysis of ovaries treated by nonlabeled peptides. The peptides assayed affected processes of egg development in 20-60% of ovarioles. The decapeptide 3d caused changes consisting in some resorbed egg chambers and normal appearance of vitellogenic eggs, whereas the octapeptide 3b caused abnormal yolk deposition and formation of big eggs with irregular yolk granules, proliferation of follicular epithelium in some egg chambers and about the same amount of resorbed egg chambers as decapeptide. These structural differences are complementary to the different values of organ radioactivities.